ID A0A2N1F9W1_9FLAO Unreviewed; 398 AA.
AC A0A2N1F9W1;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=alanine dehydrogenase {ECO:0000256|ARBA:ARBA00012897};
DE EC=1.4.1.1 {ECO:0000256|ARBA:ARBA00012897};
GN ORFNames=CXF68_13705 {ECO:0000313|EMBL:PKH51673.1};
OS Tenacibaculum sp. Bg11-29.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Tenacibaculum.
OX NCBI_TaxID=2058306 {ECO:0000313|EMBL:PKH51673.1, ECO:0000313|Proteomes:UP000233844};
RN [1] {ECO:0000313|EMBL:PKH51673.1, ECO:0000313|Proteomes:UP000233844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bg11-29 {ECO:0000313|EMBL:PKH51673.1,
RC ECO:0000313|Proteomes:UP000233844};
RA Collins E., Ducluzeau A.-L.;
RT "Pharmacopeia of the Arctic Ocean.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the AlaDH/PNT family.
CC {ECO:0000256|ARBA:ARBA00005689}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PKH51673.1}.
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DR EMBL; PJBB01000003; PKH51673.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N1F9W1; -.
DR OrthoDB; 9804592at2; -.
DR Proteomes; UP000233844; Unassembled WGS sequence.
DR GO; GO:0000286; F:alanine dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0042853; P:L-alanine catabolic process; IEA:InterPro.
DR CDD; cd05305; L-AlaDH; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR008141; Ala_DH.
DR InterPro; IPR008143; Ala_DH/PNT_CS2.
DR InterPro; IPR007886; AlaDH/PNT_N.
DR InterPro; IPR007698; AlaDH/PNT_NAD(H)-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR42795; ALANINE DEHYDROGENASE; 1.
DR PANTHER; PTHR42795:SF1; ALANINE DEHYDROGENASE 1; 1.
DR Pfam; PF01262; AlaDh_PNT_C; 1.
DR Pfam; PF05222; AlaDh_PNT_N; 1.
DR SMART; SM01002; AlaDh_PNT_C; 1.
DR SMART; SM01003; AlaDh_PNT_N; 1.
DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00837; ALADH_PNT_2; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000233844}.
FT DOMAIN 31..164
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 176..323
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 398 AA; 43509 MW; B7363D9814A2EEAE CRC64;
MGYTSPFTKE QLMPQPEMLE IKKQKGELLI GLPKETHFEE KRISLSPDAV SALVAHGHRI
VIETGAGDGA NYSDKEYSDA GAKIAYDIKE AFACTIVLKV EPPSLEEIKM LNPQTVLISA
LQLKTQDKKY FEALAKKRIT AVAFDYIKDE HGVYPIVKSL SEIAGIAAMH IAAELMTTAN
GGNGLLLGNI GGVPPSDVVI LGAGTVGEFA AKIAIGLGAR VKVFDNSITK LRKLQHFVHS
PVYTSTIQPK TLAKALMRCD VVIGAIRGKK RSPVIVTETM IEQMKDGAVI VDVSIDRGGC
FETSKITTHS KPTFNQHGVI HYCVPNIPSR YARTASVSIS NIFTPYLLNI AEEGGFENSA
RFDKSLRNGI YFYHGILTSK TVADWFDLPY RDINLLIL
//
